PFDN4

PFDN4
Identifiers
Aliases	PFDN4 , C1, PFD4, prefoldin subunit 4
External IDs	OMIM: 604898 MGI: 1923512 HomoloGene: 37645 GeneCards: PFDN4
Gene location (Human)
Chr.	Chromosome 20 (human)
End	54,228,052 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	170,361,043 bp
RNA expression pattern
	Top expressed in
	oocyte; ; ganglionic eminence; ; Achilles tendon; ; frontal pole; ; Brodmann area 10; ; superficial temporal artery; ; palpebral conjunctiva; ; secondary oocyte; ; biceps brachii; ; middle frontal gyrus;
	Top expressed in
	secondary oocyte; ; medial ganglionic eminence; ; hand; ; facial motor nucleus; ; superior cervical ganglion; ; abdominal wall; ; neural tube; ; anterior horn of spinal cord; ; primitive streak; ; maxillary prominence;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	chaperone binding ; unfolded protein binding ; protein binding ;
Cellular component	cytosol ; nucleus ; cytoplasm ; prefoldin complex ; mitochondrion ;
Biological process	protein folding ;
	Sources:Amigo / QuickGO
Orthologs
	5203
	109054
	ENSG00000101132
	ENSMUSG00000052033
	Q9NQP4
	n/a
	NM_002623
	NM_001013369 ; NM_001110152 ; NM_001199902
	NP_002614
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 18, 2022

Prefoldin subunit 4 is a protein that in humans is encoded by the PFDN4 gene.^[5]^[6]^[7]

Function

This gene encodes a member of the prefoldin beta subunit family. The encoded protein is one of six subunits of prefoldin, a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thereby allowing them to fold correctly. The complex, consisting of two alpha and four beta subunits, forms a double beta barrel assembly with six protruding coiled-coils.^[7]

Related Research Articles

Prefoldin subunit 3 (VBP-1), also Von Hippel–Lindau binding protein 1, is a prefoldin chaperone protein that binds to von Hippel–Lindau protein and transports it from perinuclear granules to the nucleus or cytoplasm inside the cell. It is also involved in transporting nascent polypeptides to cytosolic chaperonins for post-translational folding.

Prefoldin (GimC) is a superfamily of proteins used in protein folding complexes. It is classified as a heterohexameric molecular chaperone in both archaea and eukarya, including humans. A prefoldin molecule works as a transfer protein in conjunction with a molecule of chaperonin to form a chaperone complex and correctly fold other nascent proteins. One of prefoldin's main uses in eukarya is the formation of molecules of actin for use in the eukaryotic cytoskeleton.

Tubulin alpha-4A chain is a protein that in humans is encoded by the TUBA4A gene.

T-complex protein 1 subunit alpha is a protein that in humans is encoded by the TCP1 gene.

Tubulin alpha-1B chain is a protein that in humans is encoded by the TUBA1B gene.

<span class="mw-page-title-main">CCT5 (gene)</span> Protein-coding gene in the species Homo sapiens

T-complex protein 1 subunit epsilon is a protein that in humans is encoded by the CCT5 gene.

Prefoldin subunit 1 is a protein that in humans is encoded by the PFDN1 gene.

Tubulin-specific chaperone E is a protein that in humans is encoded by the TBCE gene.

Prefoldin subunit 6 is a protein that in humans is encoded by the PFDN6 gene.

Tubulin-specific chaperone D is a protein that in humans is encoded by the TBCD gene.

T-complex protein 1 subunit eta is a protein that in humans is encoded by the CCT7 gene.

T-complex protein 1 subunit delta is a protein that in humans is encoded by the CCT4 gene. The CCT4 protein is a component of the TRiC complex.

T-complex protein 1 subunit zeta is a protein that in humans is encoded by the CCT6A gene.

T-complex protein 1 subunit beta is a protein that in humans is encoded by the CCT2 gene.

Prefoldin subunit 5 is a protein that in humans is encoded by the PFDN5 gene.

T-complex protein 1 subunit gamma is a protein that in humans is encoded by the CCT3 gene.

Prefoldin subunit 2 is a protein that in humans is encoded by the PFDN2 gene.

Tubulin-specific chaperone A is a protein that in humans is encoded by the TBCA gene.

T-complex protein 1 subunit zeta-2 is a protein that in humans is encoded by the CCT6B gene.

<span class="mw-page-title-main">TRiC (complex)</span> Multiprotein complex used in cellular proteostasis

T-complex protein Ring Complex (TRiC), otherwise known as Chaperonin Containing TCP-1 (CCT), is a multiprotein complex and the chaperonin of eukaryotic cells. Like the bacterial GroEL, the TRiC complex aids in the folding of ~10% of the proteome, and actin and tubulin are some of its best known substrates. TRiC is an example of a Biological machines that folds substrates within the central cavity of its barrel-like assembly using the energy from ATP hydrolysis.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000101132 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000052033 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Vainberg IE, Lewis SA, Rommelaere H, Ampe C, Vandekerckhove J, Klein HL, Cowan NJ (May 1998). "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin". Cell. 93 (5): 863–73. doi: 10.1016/s0092-8674(00)81446-4 . PMID 9630229. S2CID 16011829.
↑ Iijima M, Kano Y, Nohno T, Namba M (Apr 1996). "Cloning of cDNA with possible transcription factor activity at the G1-S phase transition in human fibroblast cell lines". Acta Medica Okayama. 50 (2): 73–7. PMID 8744932.
1 2 Coraboeuf E, Deroubaix E, Hoerter J (May 1976). "Control of ionic permeabilities in normal and ischemic heart". Circulation Research. 38 (5 Suppl 1): I92–8. PMID 5203.

Hartl FU, Hayer-Hartl M (Mar 2002). "Molecular chaperones in the cytosol: from nascent chain to folded protein". Science. 295 (5561): 1852–8. Bibcode:2002Sci...295.1852H. doi:10.1126/science.1068408. PMID 11884745. S2CID 15037639.
Hansen WJ, Cowan NJ, Welch WJ (Apr 1999). "Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins". The Journal of Cell Biology. 145 (2): 265–77. doi:10.1083/jcb.145.2.265. PMC 2133115 . PMID 10209023.
Cowan NJ, Lewis SA (Nov 1999). "A chaperone with a hydrophilic surface". Nature Structural Biology. 6 (11): 990–1. doi:10.1038/14870. PMID 10542082. S2CID 22081346.
Collins C, Volik S, Kowbel D, Ginzinger D, Ylstra B, Cloutier T, Hawkins T, Predki P, Martin C, Wernick M, Kuo WL, Alberts A, Gray JW (Jun 2001). "Comprehensive genome sequence analysis of a breast cancer amplicon". Genome Research. 11 (6): 1034–42. doi:10.1101/gr.gr1743r. PMC 311107 . PMID 11381030.
Martín-Benito J, Boskovic J, Gómez-Puertas P, Carrascosa JL, Simons CT, Lewis SA, Bartolini F, Cowan NJ, Valpuesta JM (Dec 2002). "Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT". The EMBO Journal. 21 (23): 6377–86. doi:10.1093/emboj/cdf640. PMC 136944 . PMID 12456645.
Gstaiger M, Luke B, Hess D, Oakeley EJ, Wirbelauer C, Blondel M, Vigneron M, Peter M, Krek W (Nov 2003). "Control of nutrient-sensitive transcription programs by the unconventional prefoldin URI". Science. 302 (5648): 1208–12. Bibcode:2003Sci...302.1208G. doi:10.1126/science.1088401. PMID 14615539. S2CID 26836888.
Simons CT, Staes A, Rommelaere H, Ampe C, Lewis SA, Cowan NJ (Feb 2004). "Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding". The Journal of Biological Chemistry. 279 (6): 4196–203. doi: 10.1074/jbc.M306053200 . PMID 14634002.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000101132 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000052033 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9630229-5] Vainberg IE, Lewis SA, Rommelaere H, Ampe C, Vandekerckhove J, Klein HL, Cowan NJ (May 1998). "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin". Cell. 93 (5): 863–73. doi: 10.1016/s0092-8674(00)81446-4 . PMID 9630229. S2CID 16011829.

[pmid8744932-6] Iijima M, Kano Y, Nohno T, Namba M (Apr 1996). "Cloning of cDNA with possible transcription factor activity at the G1-S phase transition in human fibroblast cell lines". Acta Medica Okayama. 50 (2): 73–7. PMID 8744932.

[entrez-7] 1 2 Coraboeuf E, Deroubaix E, Hoerter J (May 1976). "Control of ionic permeabilities in normal and ischemic heart". Circulation Research. 38 (5 Suppl 1): I92–8. PMID 5203.

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PFDN4

Contents

Function

Related Research Articles

References

Further reading